Finding Appropriate Signal Peptides for Secretory Production of Recombinant Glucarpidase: An in Silico Method Publisher Pubmed



Vakili O¹ ; Khatami SH² ; Maleksabet A³ ; Movahedpour A^{4, 5} ; Fana SE⁶ ; Sadegh R⁷ ; Salmanzadeh AH⁷ ; Razeghifam H⁷ ; Nourdideh S⁷ ; Tehrani SS^{6, 8} ; Taherianganeh M⁴ Show Affiliations
Source: Recent Patents on Biotechnology Published:2021

Abstract

Background: Methotrexate (MTX) is a general chemotherapeutic agent utilized to treat a variety of malignancies, woefully, its high doses can cause nephrotoxicity and subsequent defect in the process of MTX excretion. The recombinant form of glucarpidase is produced by engineered E. coli and is a confirmed choice to overcoming this problem. Objective: In the present study, in silico analyses were performed to select suitable SPs for the secretion of recombinant glucarpidase in E. coli. Methods: The signal peptide website and UniProt database were employed to collect the SPs and protein sequences. In the next step, SignalP-5.0 helped us to predict the SPs and the position of cleavage sites. Moreover, physicochemical properties and solubility were evaluated using Prot-Param and Protein-sol online software, and finally, ProtCompB was used to predict the final sub-cellular localization. Results: Luckily, all SPs could form soluble fusion proteins. At last, it was found that PPB and TI-BA could translocate the glucarpidase into the extracellular compartment. Conclusion: This study showed that there are only 2 applicable SPs for the extracellular transloca-tion of glucarpidase. Although the findings were remarkable with high degrees of accuracy and pre-cision based on the utilization of bioinformatics analyses, additional experimental assessments are required to confirm and validate it. Recent patents revealed several inventions related to the clinical aspects of vaccine peptides against human disorders. © 2021 Bentham Science Publishers.